The aims of these experiments are to determine high-resolution crystal structures of a variety of enzymes in a variety of ligand states. The goal of the research is to understand the mechanism of catalysis and specificity for each enzyme. In several cases the enzymes are thought to channel products/reactants to/from other enzymes, and our studies will test these hypotheses by investigation of enzymes with amino acid substitutions engineered at various sites. We have demonstrated substantial conformational changes in some enzymes during the catalytic cycle. Understanding the regulation and coordination of conformational. change is also a goal of our structural studies. Data collected on 14-BM-C.
The aims of these experiments are to solve crystal structures of a variety of proteins by multiwavelength anomalous diffraction (MAD) using one MAD dataset from one crystal. We and others have demonstrated that MAD is the quickest way to obtain new crystal structures, given sufficient access to suitable synchrotron facilities. The motivation for structure determination for each of the proteins is to answer specific questions about function. Data collected using MAD on BioCARS Station 14-BM-C.
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| Horsman, Geoff P; Ke, Jiyuan; Dai, Shaodong et al. (2006) Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway. Biochemistry 45:11071-86 |
